Biology:Anhydro-N-acetylmuramic acid kinase: Difference between revisions
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Latest revision as of 08:06, 13 February 2024
Short description: Enzyme
| Anhydro-N-acetylmuramic acid kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.1.170 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Anhydro-N-acetylmuramic acid kinase (EC 2.7.1.170, anhMurNAc kinase, AnmK) is an enzyme with systematic name ATP:1,6-anhydro-N-acetyl-beta-muramate 6-phosphotransferase.[1][2][3] This enzyme catalyses the following chemical reaction
- ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O [math]\displaystyle{ \rightleftharpoons }[/math] ADP + N-acetylmuramate 6-phosphate
This enzyme is required for the use of anhydro-N-acetylmuramic acid in Pseudomonadota.
References
- ↑ "Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate". Journal of Bacteriology 187 (11): 3643–9. June 2005. doi:10.1128/jb.187.11.3643-3649.2005. PMID 15901686.
- ↑ "MurQ Etherase is required by Escherichia coli in order to metabolize anhydro-N-acetylmuramic acid obtained either from the environment or from its own cell wall". Journal of Bacteriology 188 (4): 1660–2. February 2006. doi:10.1128/jb.188.4.1660-1662.2006. PMID 16452451.
- ↑ "Molecular basis of 1,6-anhydro bond cleavage and phosphoryl transfer by Pseudomonas aeruginosa 1,6-anhydro-N-acetylmuramic acid kinase". The Journal of Biological Chemistry 286 (14): 12283–91. April 2011. doi:10.1074/jbc.m110.198317. PMID 21288904.
External links
- Anhydro-N-acetylmuramic+acid+kinase at the US National Library of Medicine Medical Subject Headings (MeSH)
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